Issue 24, 2014

The influence of ZnO-binding 12-mer peptides on bio-inspired ZnO formation

Abstract

ZnO precipitation experiments were carried out in a Trizma (tris(hydroxymethyl)aminomethane)-buffered aqueous solution at 37 °C and in the presence of three ZnO-binding 12-mer peptide pairs, which have nearly the same isoelectric point (pI). With this new approach, the influence of peptide sequences on ZnO mineralization under moderate conditions was investigated. Previous work was focused on electrostatic interactions between inorganic-binding peptides and inorganic surfaces. The precipitates were characterized by X-ray diffractometry (XRD), scanning electron microscopy (SEM) and X-ray photoelectron spectroscopy (XPS). Furthermore, the peptide binding to crystallographic planes of ZnO crystals was modeled by molecular dynamics (MD) simulation in explicit water. The binding free energies of all ZnO-binding peptides were calculated. The combined experimental and modeled results demonstrated a direct correlation between the binding strength of the peptide and the morphology of the ZnO particle, due to differences in their specific binding strength towards polar ZnO (001) and nonpolar (100) surfaces. As a consequence, the ZnO-binding peptides inhibited the growth of ZnO crystals by selective adsorption on the polar or nonpolar ZnO surfaces. This was demonstrated by comparison with a precipitation experiment under peptide-free conditions.

Graphical abstract: The influence of ZnO-binding 12-mer peptides on bio-inspired ZnO formation

Article information

Article type
Paper
Submitted
12 Mar 2014
Accepted
07 Apr 2014
First published
10 Apr 2014

CrystEngComm, 2014,16, 5301-5307

The influence of ZnO-binding 12-mer peptides on bio-inspired ZnO formation

J. Baier, N. J. Blumenstein, J. Preusker, L. P. H. Jeurgens, U. Welzel, T. A. Do, J. Pleiss and J. Bill, CrystEngComm, 2014, 16, 5301 DOI: 10.1039/C4CE00520A

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